› 6bdx

X-ray diffraction
1.85Å resolution

4-hydroxy tetrahydrodipicolinate reductase from Neisseria gonorrhoeae

Released:
DOI: 10.2210/pdb6bdx/pdb
PDB entry 6bdx coloured by chain, front view.
PDB entry 6bdx coloured by chain, side view.
PDB entry 6bdx coloured by chain, top view.
Source organism: Neisseria gonorrhoeae
Primary publication:
4-Hydroxy-tetrahydrodipicolinate reductase from Neisseria gonorrhoeae - structure and interactions with coenzymes and substrate analog.
Pote S, Pye SE, Sheahan TE, Gawlicka-Chruszcz A, Majorek KA, Chruszcz M
Biochem Biophys Res Commun 503 1993-1999 (2018)
PMID: 30093108

Function and Biology Details

Reaction catalysed: 
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)(+) + H(2)O = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-177056 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-hydroxy-tetrahydrodipicolinate reductase Chain: A
Molecule details ›
Chain: A
Length: 270 amino acids
Theoretical weight: 28.36 KDa
Source organism: Neisseria gonorrhoeae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5F5Y7 (Residues: 1-269; Coverage: 100%)
Gene names: NGO_1781, dapB
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 8 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: I222
Unit cell:
a: 57.803Å b: 71.723Å c: 138.414Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.169 0.21
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 citation in other articles

Comparative structural and mechanistic studies of 4-hydroxy-tetrahydrodipicolinate reductases from Mycobacterium tuberculosis and Vibrio vulnificus.
Pote et al. (2021)
1 more

1 mention without citation

4-Hydroxy-tetrahydrodipicolinate reductase from Neisseria gonorrhoeae - structure and interactions with coenzymes and substrate analog.
Pote et al. (2018)